Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Thick filaments in vertebrate striated muscles are composed of myosin heavy chain (MHC) and myosin light chains (MLCs) plus at least eight other proteins: C-protein, 86kD protein (birds) or H-protein (mammals), M-protein, myomesin, titin, MM-creatine kinase, skelemin, and AMP-deaminase. Except for CPK and AMP deaminase, none have well defined functions. Analysis of cDNA clones encoding chicken C-protein and 86kD protein has revealed a high degree of shared amino acid identity, particularly in the C-terminal 40kD. To identify functionally significant regions, the human counterpart of each protein was cloned, sequenced and analysed. Two human C-protein cDNAs were isolated with significant homology to chicken fast C-protein. Clone H75, with 69% identity to chicken fast C-protein, shows the same pattern of hybridization as the chicken fast C-protein in chicken muscles. The other clone, H8 with 60% identity, shows a pattern of hybridization in chicken muscles which is consistent with the expression of chicken slow C-protein. The human 86kD protein shares 66% DNA sequence identity with the chicken 86kD protein. Assuming that essential sequences would be conserved during evolution, we compared the chicken and human proteins using PALIGN. Chicken and human fast C-proteins possess 66% peptide identity over their deduced length plus 10% conservative substitutions. Human slow C-protein and chicken fast C-protein share 44% peptide sequence identity, plus 16% conservative substitutions. Chicken and human 86kD proteins are also very similar: 54% peptide identity plus 20% conservative substitutions. This high degree of sequence identity between chicken and human C- and 86kD proteins suggests selective pressure on the primary sequence. Recent primary sequence analyses of projectin and mini-titins from Drosophila, twitchin from C. elegans, C-protein, smMLCK, 86kD protein, and M-protein from the chicken, titin from the rabbit, and skelemin from the mouse reveals that all these proteins possess multiple internal repeats of approximately 100 amino acids. These repeating domains are of two types: one is homologous to the internal repeats which define the C-2 subset of the immunoglobulin superfamily, the other is related to the fibronectin type III repeat. Both human C-proteins possess comparable internal repeats and preliminary evidence suggests the presence of the same repeats in human 86kD. This duality of repeat structure is found in many extracellular proteins and is typified by the N-CAMs.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:cDNA cloning and sequence comparisons of human and chicken muscle C-protein and 86kD protein. 134 Oct 33

Normal (line 200) and dystrophic (line 307) embryonic chicken pectoralis muscle cells were studied in cell culture over a period of 2 weeks. During the first 4 days, normal and dystrophic cultures exhibited similar developmental increases in the number of nuclei within multinucleated myotubes, however, dystrophic muscle cells degenerated approximately twice as fast as normal cells once the initial burst of myoblast fusion was complete. The apparent synthesis rate of nonmyofibrillar proteins was similar in normal aand dystrophic cells throughout development, but the apparent synthesis rates of myosin heavy chain and the myofibrillar protein fraction were 50%--90% higher in dystrophic muscle cultures once maturity had been reached (days 6--14). The specific activities of creatine kinase and phosphofructokinase were not affected by the dystrophic condition; however, specific activity of AMP-deaminase was depressed 25%--40% in the dystrophic muscle cultures.
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PMID:Normal and dystrophic embryonic chicken pectoralis muscle cultures: I. Cell differentiation, protein synthesis, and enzyme levels. 645 4

Embryonic stem (ES) cell-derived cardiomyocytes recapitulate cardiomyogenesis in vitro and are a potential source of cells for cardiac repair. However, this requires enrichment of mixed populations of differentiating ES cells into cardiomyocytes. Toward this goal, we have generated bicistronic vectors that express both the blasticidin S deaminase (bsd) gene and a fusion protein consisting of either myosin light chain (MLC)-3f or human alpha-actinin 2A and enhanced green fluorescent protein (EGFP) under the transcriptional control of the alpha-cardiac myosin heavy chain (alpha-MHC) promoter. Insertion of the DNase I-hypersensitive site (HS)-2 element from the beta-globin locus control region, which has been shown to reduce transgene silencing in other cell systems, upstream of the transgene promoter enhanced MLC3f-EGFP gene expression levels in mouse ES cell lines. The alpha-MHC-alpha-actinin-EGFP, but not the alpha-MHC-MLC3f-EGFP, construct resulted in the correct incorporation of the newly synthesized fusion protein at the Z-band of the sarcomeres in ES cell-derived cardiomyocytes. Exposure of embryoid bodies to blasticidin S selected for a relatively pure population of cardiomyocytes within 3 days. Myofibrillogenesis could be monitored by fluorescence microscopy in living cells due to sarcomeric epitope tagging. Therefore, this genetic system permits the rapid selection of a relatively pure population of developing cardiomyocytes from a heterogeneous population of differentiating ES cells, simultaneously allowing monitoring of early myofibrillogenesis in the selected myocytes.
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PMID:Genetic selection system allowing monitoring of myofibrillogenesis in living cardiomyocytes derived from mouse embryonic stem cells. 1850 17